DNA sequence of the yeast transketolase gene

T. S. Fletcher, I. L. Kwee, T. Nakada, C. Largman, B. M. Martin

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Transketolase (EC is the enzyme that, together with aldolase, forms a reversible link between the glycolytic and pentose phosphate pathways. We have cloned and sequenced the transketolase gene from yeast (Saccharomyces cerevisiae). This is the first transketolase gene of the pentose phosphate shunt to be sequenced from any source. The molecular mass of the proposed translated protein is 73 976 daltons, in good agreement with the observed molecular mass of about 75 000 daltons. The 5'-nontranslated region of the gene is similar to other yeast genes. There is no evidence of 5'-splice junctions or branch points in the sequence. The 3'-nontranslated region contains the polyadenylation signal (AATAAA), 80 base pairs downstream from the termination codon. A high degree of homology is found between yeast transketolase and dihydroxyacetone synthase (formaldehyde transketolase) from the yeast Hansenula polymorpha. The overall sequence identity between these two proteins is 37%, with four regions of much greater similarity. The regions from amino acid residues 98-131, 157-182, 410-433, and 474-489 have sequence identities of 74%, 66%, 83%, and 82%, respectively. One of these regions (157-182) includes a possible thiamin pyrophosphate (TPP) binding domain, and another (410-433) may contain the catalytic domain.

Original languageEnglish (US)
Pages (from-to)1892-1896
Number of pages5
Issue number6
StatePublished - 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


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